Publications

Publications from current research groups. For publications from former groups, see alumni pages

2004

Histone deacetylase inhibitors up-regulate the expression of tight junction proteins.
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Mol Cancer Res, ; 2 (12): 692-701
Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks.
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Nature, ; 432 (7015): 406-411
Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive.
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Nat Cell Biol, ; 6 (11): 1122-1128
Disruption of the cingulin gene does not prevent tight junction formation but alters gene expression.
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J Cell Sci, ; 117 (Pt 22): 5245-5256
Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase.
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J Biol Chem, ; 279 (41): 42907-42915
Genome-wide lethality screen identifies new PI4,5P2 effectors that regulate the actin cytoskeleton.
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EMBO J, ; 23 (19): 3747-3757
Tethering of human Ago proteins to mRNA mimics the miRNA-mediated repression of protein synthesis.
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RNA, ; 10 (10): 1518-1525
The special Sm core structure of the U7 snRNP: far-reaching significance of a small nuclear ribonucleoprotein.
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Cell Mol Life Sci, ; 61 (19-20): 2560-2570
Defective apoptosis and B-cell lymphomas in mice with p53 point mutation at Ser 23.
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EMBO J, ; 23 (18): 3689-3699
Functional interaction between BLM helicase and 53BP1 in a Chk1-mediated pathway during S-phase arrest.
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J Cell Biol, ; 166 (6): 801-813
Constitutively active DNA damage checkpoint pathways as the driving force for the high frequency of p53 mutations in human cancer.
DNA Repair (Amst), ; 3 (8-9): 1057-1062
53BP1, an activator of ATM in response to DNA damage.
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DNA Repair (Amst), ; 3 (8-9): 945-952
Structural differences in the DNA binding domains of human p53 and its C. elegans ortholog Cep-1.
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Structure, ; 12 (7): 1237-1243
Altered active site flexibility and a structural metal-binding site in eukaryotic dUTPase: kinetic characterization, folding, and crystallographic studies of the homotrimeric Drosophila enzyme.
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J Biol Chem, ; 279 (17): 17932-17944
p53 and stress in the ER.
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Genes Dev, ; 18 (3): 241-244